2.0 Angstrom Crystal Structure of Manganese Protoporphyrin IX-reconstituted Ovine Prostaglandin H2 Synthase-1 Complexed With Flurbiprofen. Determined by X-ray diffraction at 2.0 Å resolution. Released 24 Jan 2006.
Explore 2AYL in 3D Show helices and sheets RCSB PDB PDBe
2AYL contains 90 α-helices and 60 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 35-38 | 4 | |
| α-helix | 45 | 1 | |
| β-strand | 46-50 | 5 | 1 |
| β-strand | 54-58 | 5 | 1 |
| β-strand | 64-65 | 2 | 2 |
| β-strand | 71-72 | 2 | 2 |
| α-helix | 74-82 | 9 | |
| α-helix | 83-85 | 3 | |
| α-helix | 86-93 | 8 | |
| α-helix | 97-103 | 7 | |
| α-helix | 108-121 | 14 | |
| β-strand | 130-131 | 2 | 3 |
| α-helix | 139-143 | 5 | |
| β-strand | 147 | 1 | 4 |
| β-strand | 149-150 | 2 | 3 |
| α-helix | 153-156 | 4 | |
| β-strand | 161 | 1 | 5 |
| β-strand | 164 | 1 | 5 |
| α-helix | 171-173 | 3 | |
| α-helix | 174-181 | 8 | |
| β-strand | 183 | 1 | 6 |
| β-strand | 189 | 1 | 7 |
| β-strand | 194 | 1 | 8 |
| β-strand | 195 | 1 | 9 |
| α-helix | 196-206 | 11 | |
| β-strand | 212 | 1 | 10 |
| β-strand | 220 | 1 | 4 |
| β-strand | 221 | 1 | 10 |
| α-helix | 231-234 | 4 | |
| α-helix | 238-244 | 7 | |
| β-strand | 245 | 1 | 11 |
| α-helix | 251 | 1 | |
| β-strand | 252 | 1 | 11 |
| α-helix | 253 | 1 | |
| β-strand | 255-257 | 3 | 12 |
| β-strand | 260-262 | 3 | 12 |
| α-helix | 263-264 | 2 | |
| β-strand | 265 | 1 | 13 |
| α-helix | 281-283 | 3 | |
| β-strand | 285 | 1 | 13 |
| α-helix | 292-294 | 3 | |
| α-helix | 296-319 | 24 | |
| α-helix | 325-343 | 19 | |
| α-helix | 344-348 | 5 | |
| α-helix | 349-353 | 5 | |
| α-helix | 363-366 | 4 | |
| β-strand | 378 | 1 | 3 |
| α-helix | 379-384 | 6 | |
| α-helix | 388-390 | 3 | |
| β-strand | 395-397 | 3 | 14 |
| β-strand | 400-402 | 3 | 14 |
| α-helix | 404-407 | 4 | |
| α-helix | 413-428 | 16 | |
| β-strand | 430 | 1 | 9 |
| α-helix | 431 | 1 | |
| β-strand | 432 | 1 | 7 |
| α-helix | 433 | 1 | |
| β-strand | 440 | 1 | 6 |
| α-helix | 442-444 | 3 | |
| α-helix | 445-458 | 14 | |
| α-helix | 460-461 | 2 | |
| β-strand | 462 | 1 | 15 |
| α-helix | 463-469 | 7 | |
| α-helix | 473-475 | 3 | |
| α-helix | 478-482 | 5 | |
| α-helix | 486-495 | 10 | |
| α-helix | 498-500 | 3 | |
| β-strand | 502 | 1 | 15 |
| α-helix | 503-509 | 7 | |
| α-helix | 511-513 | 3 | |
| α-helix | 520-535 | 16 | |
| α-helix | 538-540 | 3 | |
| α-helix | 547-550 | 4 | |
| α-helix | 553-560 | 8 | |
| α-helix | 564-569 | 6 | |
| β-strand | 581 | 1 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1035-1038 | 4 | |
| α-helix | 1045 | 1 | |
| β-strand | 1046-1050 | 5 | 16 |
| β-strand | 1054-1058 | 5 | 16 |
| β-strand | 1064-1065 | 2 | 17 |
| β-strand | 1071-1072 | 2 | 17 |
| α-helix | 1074-1082 | 9 | |
| α-helix | 1083-1085 | 3 | |
| α-helix | 1086-1093 | 8 | |
| α-helix | 1097-1104 | 8 | |
| α-helix | 1108-1121 | 14 | |
| β-strand | 1130-1131 | 2 | 18 |
| α-helix | 1139-1143 | 5 | |
| β-strand | 1147 | 1 | 19 |
| β-strand | 1149-1150 | 2 | 18 |
| α-helix | 1153-1156 | 4 | |
| β-strand | 1161 | 1 | 20 |
| β-strand | 1164 | 1 | 20 |
| α-helix | 1171-1173 | 3 | |
| α-helix | 1174-1181 | 8 | |
| β-strand | 1183 | 1 | 21 |
| β-strand | 1189 | 1 | 22 |
| β-strand | 1194 | 1 | 23 |
| β-strand | 1195 | 1 | 24 |
| α-helix | 1196-1206 | 11 | |
| β-strand | 1212 | 1 | 25 |
| β-strand | 1220 | 1 | 19 |
| β-strand | 1221 | 1 | 25 |
| α-helix | 1231-1234 | 4 | |
| α-helix | 1238-1244 | 7 | |
| β-strand | 1245 | 1 | 26 |
| α-helix | 1251 | 1 | |
| β-strand | 1252 | 1 | 26 |
| α-helix | 1253 | 1 | |
| β-strand | 1255-1257 | 3 | 27 |
| β-strand | 1260-1262 | 3 | 27 |
| α-helix | 1263-1264 | 2 | |
| β-strand | 1265 | 1 | 28 |
| α-helix | 1281-1283 | 3 | |
| β-strand | 1285 | 1 | 28 |
| α-helix | 1292-1294 | 3 | |
| α-helix | 1296-1319 | 24 | |
| α-helix | 1325-1343 | 19 | |
| α-helix | 1344-1348 | 5 | |
| α-helix | 1349-1353 | 5 | |
| α-helix | 1363-1366 | 4 | |
| β-strand | 1378 | 1 | 18 |
| α-helix | 1379-1384 | 6 | |
| α-helix | 1388-1390 | 3 | |
| β-strand | 1395-1397 | 3 | 29 |
| β-strand | 1400-1402 | 3 | 29 |
| α-helix | 1404-1407 | 4 | |
| α-helix | 1413-1428 | 16 | |
| β-strand | 1430 | 1 | 24 |
| α-helix | 1431 | 1 | |
| β-strand | 1432 | 1 | 22 |
| α-helix | 1433 | 1 | |
| β-strand | 1440 | 1 | 21 |
| α-helix | 1442-1444 | 3 | |
| α-helix | 1445-1457 | 13 | |
| α-helix | 1460-1462 | 3 | |
| α-helix | 1463-1469 | 7 | |
| α-helix | 1473-1475 | 3 | |
| α-helix | 1478-1482 | 5 | |
| α-helix | 1486-1495 | 10 | |
| α-helix | 1498-1500 | 3 | |
| α-helix | 1503-1509 | 7 | |
| α-helix | 1511-1513 | 3 | |
| α-helix | 1520-1535 | 16 | |
| α-helix | 1538-1540 | 3 | |
| α-helix | 1547-1550 | 4 | |
| α-helix | 1553-1560 | 8 | |
| α-helix | 1564-1569 | 6 | |
| β-strand | 1581 | 1 | 23 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Prostaglandin G/H synthase 1 | A, B | protein | 553 | Ovis aries | P05979 (AlphaFold model) |
>2AYL_1 Prostaglandin G/H synthase 1 (chains A, B) PVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPEIWTWLRTTLRPSPSFIHF LLTHGRWLWDFVNATFIRDTLMRLVLTVRSNLIPSPPTYNIAHDYISWESFSNVSYYTRI LPSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFK TSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPV LMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATIWLREHNRVCDLLKAEHPTWGDEQLFQT ARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPLM PDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPAGRIGGGRNIDHHILHVAVDV IKESRVLRLQPFNEYRKRFGMKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEK CHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFGGEVGFNLVKTATLKKLVCLN TKTCPYVSFHVPD
| ID | Name | Formula | Copies |
|---|---|---|---|
| BOG | octyl beta-D-glucopyranoside | C14 H28 O6 | 7 |
| FLP | Flurbiprofen | C15 H13 F O2 | 2 |
| MNH | Manganese protoporphyrin IX | C34 H32 Mn N4 O4 | 2 |
Water and common crystallization additives (GOL) are not listed.
2.0 angstroms structure of prostaglandin H2 synthase-1 reconstituted with a manganese porphyrin cofactor. Gupta, K., Selinsky, B.S., Loll, P.J. Acta Crystallogr D Biol Crystallogr (2006) 62:151-156. DOI 10.1107/S0907444905036309 · PubMed
Other PDB entries of the same protein (UniProt P05979 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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